deamidase

Other names in common use include 4-methyleneglutamine deamidase, and 4-methyleneglutamine amidohydrolase.

Besides its transglutaminase activity, tTG is proposed to also act as kinase, and protein disulfide isomerase, and deamidase.

Therefore, gluten is often modified for commercial use by deamidation by treatment with acid at high temperatures, or enzymatic treatment with deamidase or transglutaminases.

While prolamins and glutelins are excellent deamidase and transaminase substrates the highly repetitive motifs, particularly polyproline/glutamine tracts, are often poor substrates for gastroentestinal endoproteases, such as those produced in the GI tract.

OspI has glutamine deamidase activity, and is able to selectively deaminate glutamine at position 100 in UBC13 to glutamate and this results in a failure of the E2 ubiquitin-conjugating activity which is required for TRAF6 activation.